Mcl-1(128-350) fragment induces apoptosis through direct interaction with Bax

作者：Menoret Emmanuelle; Gomez Bougie Patricia; Surget Sylvanie; Trichet Valerie; Oliver Lisa; Pellat Deceunynck Catherine; Amiot Martine^*

来源：FEBS Letters, 2010, 584(3): 487-492.

DOI：10.1016/j.febslet.2009.11.094

• Mcl-1
• Cleaved Mcl-1
• Bax activation

Mcl-1 full-length (Mcl-1(1-350)), a tightly regulated protein, plays an important role in protecting cells against apoptosis. Cleavage of Mcl-1 at Asp127 by caspase (Mcl-1(C1)) contributes to the regulation of Mcl-1 expression, but its pro-apoptotic function remains controversial. Here, we reported that Mcl-1(128-350) expression induced caspase-dependent apoptosis. We demonstrated that Mcl-1(128-350) but not Mcl-1(1-350) interacts with Bax. This interaction required an intact BH3 Mcl-1(128-350) domain and leads to Bax activation and translocation to mitochondria. The silencing of Bax, but not of Bak, prevented Mcl-1(128-350) induced apoptosis. In conclusion, Mcl-1(128-350) exerts a pro-apoptotic function governed by its capacity to interact with Bax.

• 出版日期2010-2-5